ArticleCancer biology & therapy2019
UNC-45A is preferentially expressed in epithelial cells and binds to and co-localizes with interphase MTs.
Article in Cancer biology & therapy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- A prognostic gene signature derived from aging-related genes predicts survival, immune landscape and therapy response in glioma.Molecular and clinical oncology · 2026Article
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Unveiling the novel value of TREM1 in the proneural-mesenchymal transition of glioma via tumor-associated macrophages.Frontiers in immunology · 2025Article
- Review
- Review
- The Ovary-Brain Connection.Cells · 2024Article
- Article
- A myosin chaperone, UNC-45A, is a novel regulator of intestinal epithelial barrier integrity and repair.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Article
- UNC-45A breaks the microtubule lattice independently of its effects on non-muscle myosin II.Journal of cell science · 2021Article
- Mechanisms of Taxane ResistanceCancers · 2020Review
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
UNC-45A is an ubiquitously expressed protein highly conserved throughout evolution. Most of what we currently know about UNC-45A pertains to its role as a regulator of the actomyosin system. However, emerging studies from both our and other laboratories support a role of UNC-45A outside of actomyosin regulation. This includes studies showing that UNC-45A: regulates gene transcription, co-localizes and biochemically co-fractionates with gamma tubulin and regulates centrosomal positioning, is found in the same subcellular fractions where MT-associated proteins are, and is a mitotic spindle-associated protein with MT-destabilizing activity in absence of the actomyosin system. Here, we extended our previous findings and show that UNC45A is variably expressed across a spectrum of cell lines with the highest level being found in HeLa cells and in ovarian cancer cells inherently paclitaxel-resistant. Furthermore, we show that UNC-45A is preferentially expressed in epithelial cells, localizes to mitotic spindles in clinical tumor specimens of cancer and co-localizes and co-fractionates with MTs in interphase cells independent of actin or myosin. In sum, we report alteration of UNC45A localization in the setting of chemotherapeutic treatment of cells with paclitaxel, and localization of UNC45A to MTs both
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